Biological Magnetic Resonance Volume 3

1 Multiple Irradiation 1H NMR Experiments with Hemoproteins.- 1. Introduction.- 1.1. Structure and Biological Functions of Hemoproteins.- 1.2. 1H NMR Spectra of Hemoproteins.- 1.3. 1H NMR Spectra of Isolated Heme Groups.- 1.4. Purpose of This Review.- 2. Use of Multiple Irradiation 1H NMR Techniques.- 2.1. Double Irradiation Difference Spectra.- 2.2. Spin Decoupling.- 2.3. Saturation Transfer.- 2.4. Nuclear Overhauser Enhancement and Spin Diffusion.- 2.5. Two-Dimensional NMR.- 3. Studies of the Heme Groups and the Axial Ligands of the Heme Iron.- 3.1. Individual Assignments of the Heme Proton Resonances.- 3.2. Survey of Heme c1H NMR Data Obtained with Various Cytochromes c.- 3.3. Studies of the Axial Ligands in Cytochromes c.- 4. Studies of Aromatic Amino Acid Residues.- 4.1. High-Resolution 1H NMR and Internal Mobility of Aromatic Rings.- 4.2. Identification of Aromatic Spin Systems in Hemoproteins.- 4.3. Survey of Results Obtained for c-Type Cytochromes.- 5. Nuclear Overhauser Effects for Studies of Nonbonding Heme-Polypeptide Interactions.- 5.1. Orientation of the Heme Group in Cytochrome b5.- References.- 2 Vanadyl(IV) EPR Spin Probes: Inorganic and Biochemical Aspects.- 1. Introduction.- 2. Inorganic Chemistry and Spectroscopy of the Vanadyl Ion.- 2.1. Geometries and Stabilities of Coordination Complexes.- 2.2. Optical Spectral Properties.- 2.3. EPR Spectral Properties.- 2.4. Analysis of EPR Spectra of Frozen Solution Samples.- 2.5. Measurement of Rotational Correlation Times.- 2.6. Model Compound Studies.- 3. Protein Studies.- 3.1. The Transferrins.- 3.2. Bovine Insulin.- 3.3. Bovine Carbonic Anhydrase.- 3.4. Bovine Carboxypeptidase A.- 3.5. Bovine Serum Albumin.- 3.6. Nucleases and Phosphatases.- 3.7. Experimental Techniques.- 4. Biomineralization Processes.- 5. Nucleic Acids.- 6. Biological Vanadium.- 6.1. Regulation of Cation Transport in Mammalian Systems.- 6.2. Other Systems.- 7. Liquid Crystals and Micelles.- 8. Biogeochemical Studies.- 8.1. Petroleum Deposits.- 8.2. Humic and Fulvic Acids.- 8.3. Adsorption Studies.- 9. A Look to the Future.- References.- 3 ESR Studies of Calcium- and Proton-Induced Phase Separations in Phosphatidylserine-Phosphatidylcholine Mixed Membranes.- 1. Introduction-Spin Probe (ESR) Applications to Membrane Studies.- 2. Examples of ESR Spectral Changes Associated with PC* Clustering or Concentration in Membranes.- 3. Ca2+-Induced Phase Separation in PS-PC Membranes.- 3.1. Experimental Aspects-Membrane Preparation on a Millipore Filter Pore Surface.- 3.2. Crystallization of PS in the Membranes.- 3.3. Phase Diagram of PS-PC Membranes in the Presence of Ca2+.- 3.4. Concentration of Ca2+ Required for the Phase Separation.- 3.5. Selectivity for Divalent Cations and Competition with Local Anesthetic.- 3.6. Rate of Phase Separation.- 4. H+-Induced Phase Separation in PS-PC Membranes.- 4.1. Phase Separation on Lowering pH.- 4.2. Phase Separation on Decreasing Salt Concentration.- 5. Disappearance of Ca2+-Induced Phase Separation in PS-PC Membranes.- 5.1. Replacement of Ca2+ with H+ in Acidic or Low-Ionic- Strength Media.- 5.2. Disappearance in Nonbuffered Salt Solution.- 6. Ca2+-Induced Phase Separation in PA-PC Membranes.- 7. Discussion.- 7.1. Surface Hydrophobicity Caused by Ca2+ Binding as a Driving Force for the Phase Separation.- 7.2. Characteristic Difference between Ca2+ and Mg2+ for PS-PC Membranes.- 7.3. Are the Phase Separations Lateral?.- 7.4. Biological Significance.- References.- 4 EPR Crystallography of Metalloproteins and Spin-Labeled Enzymes.- 1. Introduction.- 2. Experimental Methods and Procedures.- 2.1. Growing Crystals.- 2.2. Mixed Crystals.- 2.3. Handling Protein Crystals.- 2.4. Isotopic Labeling.- 2.5. Spin Labeling.- 2.6. Crystal Type.- 2.7. Goniometer.- 2.8. Mounting.- 2.9. Data Acquisition.- 3. Data Processing.- 3.1. Theory.- 3.2. Diagonalization.- 3.3. Other EPR Tensors.- 4. EPR Theory.- 4.1. General Spin Hamiltonians.- 4.2. g Tensor.- 4.3. Hyperfine Tensor.- 4.4. Superhyperfine Tensor.- 4.5. Ab Initio Calculations.- 4.6. Spin Labels.- 5. Structure Determinations.- 5.1. g Tensor and Heme Plane Orientation.- 5.2. Stereochemistry of Ligand Binding.- 5.3. Unpaired Spin Density Distribution and Electron Structure.- 5.4. Zero-Field Splitting.- 5.5. Protein Fine Structure by Spin Labeling.- 5.6. Active Site Structure.- 6. Lattice Disorder.- 7. Molecular Dynamics.- 8. Miscellaneous Studies.- 9. Appendix.- 9.1. Complete Working Version of ANL208E and Subroutines MATINV, FUNC, and ZIPPO for Least Squares Fitting of N sets of (gi2, ?i) for One Plane.- 9.2. Subroutine FUNC.- 9.3. Subroutine MATINV.- 9.4. Subroutine ZIPPO.- 9.5. Sample Data Deck.- 9.6. Sample Program Output for KEYSS = 1.- 9.7. Data Deck Description.- References.- 5 Electron Spin Echo Spectroscopy and the Study of Metalloproteins.- 1. Introduction.- 2. The Design of Electron Spin Echo Experiments.- 2.1. The Time Scale.- 2.2. The Microwave Transmitter.- 2.3. The Microwave Receiver.- 2.4. Cavity Design.- 2.5. Sensitivity: Comparison's with c.w. Spectroscopy.- 2.6. Temperature and Magnetic Concentrations in Electron Spin Echo Experiments.- 2.7. Choice of Experimental Frequency Range.- 3. Echo Envelope Spectroscopy.- 3.1. The Two-Pulse Echo Envelope.- 3.2. Factoring Contributions Due to Several Nuclei.- 3.3. The Three-Pulse Echo Envelope.- 3.4. Fourier Transformation of the Echo Envelope.- 3.5. Echo Envelope Spectroscopy and ENDOR.- 4. The Detection of Small Perturbations.- 4.1. ENDOR by Spin Echoes.- 4.2. Electric-Field-Induced Shifts.- 4.3. The Detection of Weak Coupling between Electron Spins.- 5. Measurement of the Spin-Lattice Relaxation Time T1.- 6. Summary.- References.